//
sign in
Profile
by @danabra.mov
Profile
by @dansshadow.bsky.social
Profile
by @jimpick.com
AviHandle
by @danabra.mov
AviHandle
by @dansshadow.bsky.social
AviHandle
by @katherine.computer
EventsList
by @katherine.computer
ProfileHeader
by @dansshadow.bsky.social
ProfileHeader
by @danabra.mov
ProfileMedia
by @danabra.mov
ProfilePlays
by @danabra.mov
ProfilePosts
by @danabra.mov
ProfilePosts
by @dansshadow.bsky.social
ProfileReplies
by @danabra.mov
Record
by @atsui.org
Skircle
by @danabra.mov
StreamPlacePlaylist
by @katherine.computer
+ new component
Profile
Loading...
Laboratory of Pietro De Camilli - Department of Neuroscience at Yale University
De Camilli Lab


"Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C" out now in PLOS Biology journals.plos.org/plosbiology/...
8mo
"The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage" out now in Nature Cell Biology rdcu.be/ehbaL
Apr 10, 2025
De Camilli Lab
Nature Cell Biology - Wang et al. show the recruitment of the lipid channel protein VPS13C and formation of VPS13C-dependent contacts between endoplasmic reticulum and lysosomes after lysosomal...
rdcu.be
The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage
De Camilli Lab
VPS13A and VPS13C are bridge-like lipid transport proteins with distinct subcellular localization and function, and their absence is linked with chorea-acanthocytosis and Parkinson's disease, respecti...
journals.plos.org
Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C
New research from @pdc-lab.bsky.social & collaborators finds that the bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage; #Parkinsons-associated LRRK2 is also recruited but at later stage www.nature.com/articles/s41...
Apr 10, 2025
The Science of Parkinson's